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Nandadasa S, Burin des Roziers C, Koch C, et al. A new mouse mutant with cleavage-resistant versican and isoform-specific versican mutants demonstrate that proteolysis at the Glu. Matrix Biol Plus. 2021;10:100064doi: 10.1016/j.mbplus.2021.100064.
Nandadasa, S., Burin des Roziers, C., Koch, C., Tran-Lundmark, K., Dours-Zimmermann, M. T., Zimmermann, D. R., Valleix, S., & Apte, S. S. (2021). A new mouse mutant with cleavage-resistant versican and isoform-specific versican mutants demonstrate that proteolysis at the Glu. Matrix biology plus, 10100064. https://doi.org/10.1016/j.mbplus.2021.100064
Nandadasa, Sumeda, et al. "A new mouse mutant with cleavage-resistant versican and isoform-specific versican mutants demonstrate that proteolysis at the Glu." Matrix biology plus vol. 10 (2021): 100064. doi: https://doi.org/10.1016/j.mbplus.2021.100064
Nandadasa S, Burin des Roziers C, Koch C, Tran-Lundmark K, Dours-Zimmermann MT, Zimmermann DR, Valleix S, Apte SS. A new mouse mutant with cleavage-resistant versican and isoform-specific versican mutants demonstrate that proteolysis at the Glu. Matrix Biol Plus. 2021 May 14;10:100064. doi: 10.1016/j.mbplus.2021.100064. eCollection 2021 Jun. PMID: 34195596; PMCID: PMC8233476.
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Matrix Biol Plus. 2021 May 14;10:100064. doi: 10.1016/j.mbplus.2021.100064. eCollection 2021 Jun.

A new mouse mutant with cleavage-resistant versican and isoform-specific versican mutants demonstrate that proteolysis at the Glu.

Matrix biology plus

Sumeda Nandadasa, Cyril Burin des Roziers, Christopher Koch, Karin Tran-Lundmark, María T Dours-Zimmermann, Dieter R Zimmermann, Sophie Valleix, Suneel S Apte

Affiliations

  1. Department of Biomedical Engineering-ND20, Cleveland Clinic Lerner Research Institute, 9500 Euclid Avenue, Cleveland, OH 44195, United States.
  2. Institut Cochin, Inserm U1016 - CNRS UMR8104 - Paris Descartes University Medical School, 24, Rue du faubourg Saint Jacques, 75014 Paris, France.
  3. Department of Experimental Medical Science and Wallenberg Center for Molecular Medicine, Lund University, Lund, Sweden.
  4. Department of Pathology and Molecular Pathology, University Hospital Zurich, Zurich, Switzerland.

PMID: 34195596 PMCID: PMC8233476 DOI: 10.1016/j.mbplus.2021.100064

Abstract

Two inherent challenges in the mechanistic interpretation of protease-deficient phenotypes are defining the specific substrate cleavages whose reduction generates the phenotypes and determining whether the phenotypes result from loss of substrate function, substrate accumulation, or loss of a function(s) embodied in the substrate fragments. Hence, recapitulation of a protease-deficient phenotype by a cleavage-resistant substrate would stringently validate the importance of a proteolytic event and clarify the underlying mechanisms. Versican is a large proteoglycan required for development of the circulatory system and proper limb development, and is cleaved by ADAMTS proteases at the Glu

© 2021 The Authors. Published by Elsevier B.V.

Keywords: ADAMTS; Extracellular matrix; Limb development; Metalloprotease; Proteoglycan; Syndactyly

Conflict of interest statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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